17 research outputs found
Surfactant protein B polymorphisms are associated with severe respiratory syncytial virus infection, but not with asthma
Exogenous porcine surfactant (Curosurf) is inactivated by monoclonal antibody to the surfactant-associated hydrophobic protein SP-B
Efficacy of Synthetic Peptide-Containing Surfactant in the Treatment of Respiratory Distress Syndrome in Preterm Infant Rhesus Monkeys
Treatment Responses to Surfactants Containing Natural Surfactant Proteins in Preterm Rabbits
Protein Composition of Synthetic Surfactant Affects Gas Exchange in Surfactant-Deficient Rats
Surfactant protein levels in bronchoalveolar lavage after segmental allergen challenge in patients with asthma
Surfactant Protein B Corrects Oxygen-Induced Pulmonary Dysfunction in Heterozygous Surfactant Protein B–Deficient Mice
Role of the N-Terminal Seven Residues of Surfactant Protein B (SP-B)
Breathing is enabled by lung surfactant, a mixture of proteins and lipids that forms a surface-active layer and reduces surface tension at the air-water interface in lungs. Surfactant protein B (SP-B) is an essential component of lung surfactant. In this study we probe the mechanism underlying the important functional contributions made by the N-terminal 7 residues of SP-B, a region sometimes called the “insertion sequence”. These studies employed a construct of SP-B, SP-B (1–25,63–78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B. Circular dichroism, solution NMR, and solid state 2H NMR were used to study the structure of SP-B (1–25,63–78) and its interactions with phospholipid bilayers. Comparison of results for SP-B (8–25,63–78) and SP-B (1–25,63–78) demonstrates that the presence of the 7-residue insertion sequence induces substantial disorder near the centre of the lipid bilayer, but without a major disruption of the overall mechanical orientation of the bilayers. This observation suggests the insertion sequence is unlikely to penetrate deeply into the bilayer. The 7-residue insertion sequence substantially increases the solution NMR linewidths, most likely due to an increase in global dynamics